Table 5.
Check of Predictions Against Actual Measurements
| Entry | Enzyme | Thermostable species | Point | Result |
|---|---|---|---|---|
| 1 | 2-Oxoglutarate dehydrogenase | C. efficiens | 0 | — |
| 2 | Glutamate dehydrogenase | C. efficiens | 1 | Yes |
| 3 | Isocitrate lyase | C. efficiens | 2 | Yes |
| 4 | Phosphofructokinase | C. efficiens | -3 | No |
| 5 | Fructose-1-phosphate kinase | C. efficiens | 5 | Yes |
| 6 | Isocitrate dehydrogenase | C. efficiens | 4 | Yes |
| 7 | Aconitase | C. efficiens | 0 | — |
| 8 | Phosphoenolpyruvate carboxylase | C. efficiens | 10 | Yes |
| 9 | Citrate synthase | C. efficiens | 3 | Yes |
| 10 | Aspartate kinase | C. glutamicum | -1 | Yes |
| 11 | Dihydrodipicolinate synthase | C. efficiens | 0 | — |
| 12 | Diaminopimelate dehydrogenase | C. glutamicum | -2 | Yes |
| 13 | Diaminopimelate decarboxylase | C. efficiens | 2 | Yes |
Point is defined as the difference between the sum of the three kinds of substitutions from C. glutamicum to C. efficiens (Lys to Arg, Ser to Ala and Ser to Thr) and the sum of the reverse substitutions (Point = {number of (Lys → Arg + Ser → Ala + Ser → Thr)} - {number of (Arg → Lys + Ala → Ser + Thr → Ser)})
Results are indicated by (1) Yes: when the enzyme from C. efficiens was more thermostable and the point is positive, or when the enzyme from C. glutamicum was more thermostable and point is negative. (2) —: when the point value was zero. (3) No: all other cases